The Experts below are selected from a list of 2922 Experts worldwide ranked by ideXlab platform

Kathryn W Peters - One of the best experts on this subject based on the ideXlab platform.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

Huamin Wang - One of the best experts on this subject based on the ideXlab platform.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

Linton M Traub - One of the best experts on this subject based on the ideXlab platform.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

  • Clathrin Adaptor Proteins in Cargo Endocytosis
    Endosomes, 1
    Co-Authors: Linton M Traub
    Abstract:

    Eukaryotic cells continuously remodel the protein and lipid composition of the plasma membrane in response to the extracellular milieu. Membrane retrieval typically involves inward budding of small bilayer-encapsulated vesicles that shuttle protein and lipid from the surface to internal endosomal elements. Clathrin-mediated endocytosis is a dominant pathway for internalization in many cell types, and a range of dedicated signals are used to ensure selective sorting in this pathway. Evidence suggests that the Clathrin coat utilizes a diverse collection of Clathrin-associated sorting Proteins (CLASPs) to ensure the efficient and noncompetitive concentration of a wide variety of sorting signals within transport vesicles forming at the cell surface.

Robert S. Edinger - One of the best experts on this subject based on the ideXlab platform.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

Michael B. Butterworth - One of the best experts on this subject based on the ideXlab platform.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.

  • Clathrin mediated endocytosis of the epithelial sodium channel role of epsin
    Journal of Biological Chemistry, 2006
    Co-Authors: Huamin Wang, Linton M Traub, Kelly M Weixel, Matthew J Hawryluk, Nirav Shah, Lauren Kester, Clint J Perry, Michael B. Butterworth, Robert S. Edinger, Kathryn W Peters
    Abstract:

    Abstract Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in Clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and Clathrin Adaptor Proteins, and epsin, as expected, co-immunoprecipitates with Clathrin Adaptor Proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the Clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.